Evidence map›Paper›PMID 29444410›Full record

ArticleAnalytical chemistry2018

Enhanced Ion Transmission Efficiency up to m/ z 24 000 for MALDI Protein Imaging Mass Spectrometry.

Boone M Prentice, Daniel J Ryan, Raf Van de Plas, Richard M Caprioli, Jeffrey M Spraggins

Abstract read
In one paragraph

Article in Analytical chemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed, 1 pooled it
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

22 citing papers in PubMed, 1 synthesis or guideline pooled it.

  1. Pooled it
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Review
  8. Journal of the American Society for Mass Spectrometry · 2023
    Article
  9. Review
  10. Review
  11. Article
  12. Article
  13. Article
  14. Proteoform-Selective Imaging of Tissues Using Mass Spectrometry.Angewandte Chemie (International ed. in English) · 2022
    Article
  15. Review
  16. Review
  17. Article
  18. Article
  19. Article
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

5 authors.

Raf Van de PlasDelft Center for Systems and Control , Delft University of Technology , Delft 2628 CD , The Netherlands.ORCID 0000-0002-2232-7130
Richard M CaprioliORCID 0000-0001-5859-3310
Jeffrey M SpragginsORCID 0000-0001-9198-5498

Funding

Training (pp 214-245)P41GM103391 · NIGMS · VANDERBILT UNIVERSITY · PI CAPRIOLI, RICHARD M · 2012 to 2020
$17.7M
15 Tesla Bruker SolariX FT-ICR mass spectrometerS10OD012359 · OD · VANDERBILT UNIVERSITY · PI CAPRIOLI, RICHARD M · 2012 to 2012
$1.6M
NIGMS NIH HHS P41 GM103391NIH HHS S10 OD012359
6 · The paper itself

Abstract

The molecular identification of species of interest is an important part of an imaging mass spectrometry (IMS) experiment. The high resolution accurate mass capabilities of Fourier transform ion cyclotron resonance mass spectrometry (FT-ICR MS) have recently been shown to facilitate the identification of proteins in matrix-assisted laser desorption/ionization (MALDI) IMS. However, these experiments are typically limited to proteins giving rise to ions of relatively low m/ z due to difficulties transmitting and measuring large molecular weight ions of low charge states. Herein we have modified the source gas manifold of a commercial MALDI FT-ICR MS to regulate the gas flow and pressure to maximize the transmission of large m/ z protein ions through the ion funnel region of the instrument. By minimizing the contribution of off-axis gas disruption to ion focusing and maximizing the effective potential wall confining the ions through pressure optimization, the signal-to-noise ratios (S/N) of most protein species were improved by roughly 1 order of magnitude compared to normal source conditions. These modifications enabled the detection of protein standards up to m/ z 24 000 and the detection of proteins from tissue up to m/ z 22 000 with good S/N, roughly doubling the mass range for which high quality protein ion images from rat brain and kidney tissue could be produced. Due to the long time-domain transients (>4 s) required to isotopically resolve high m/ z proteins, we have used these data as part of an FT-ICR IMS-microscopy data-driven image fusion workflow to produce estimated protein images with both high mass and high spatial resolutions.

Indexed as

AnimalsApoproteinsBrainIonsKidneyMolecular WeightMyoglobinProteinsRatsSignal-To-Noise RatioSpectrometry, Mass, Matrix-Assisted Laser Desorption-IonizationUbiquitinapomyoglobinApoproteinsIonsMyoglobinProteinsUbiquitin

Identifiers

PMID29444410
PMCPMC6905630

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Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.